Evidence map›Paper›PMID 24667272›Full record

ArticleNature communications2014

Dido3-dependent HDAC6 targeting controls cilium size.

Ainhoa Sánchez de Diego, Astrid Alonso Guerrero, Carlos Martínez-A, Karel H M van Wely

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 50 citations in OpenAlex.

  1. Post-Translational Modifications in Cilia and Ciliopathies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
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  10. Primary cilium and its role in tumorigenesis.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2021
    Article
  11. Article
  12. Primary Cilia and Atherosclerosis.Frontiers in physiology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Primary Cilia as Signaling Hubs in Health and Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Review
  17. A microfluidic device forBiomicrofluidics · 2019
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Ainhoa Sánchez de DiegoDepartment of Immunology and Oncology, Centro Nacional de Biotecnología (CNB-CSIC), C/Darwin 3, Campus UAM Cantoblanco, 28049 Madrid, Spain.
Astrid Alonso GuerreroDepartment of Immunology and Oncology, Centro Nacional de Biotecnología (CNB-CSIC), C/Darwin 3, Campus UAM Cantoblanco, 28049 Madrid, Spain.
Carlos Martínez-ADepartment of Immunology and Oncology, Centro Nacional de Biotecnología (CNB-CSIC), C/Darwin 3, Campus UAM Cantoblanco, 28049 Madrid, Spain.
Karel H M van WelyDepartment of Immunology and Oncology, Centro Nacional de Biotecnología (CNB-CSIC), C/Darwin 3, Campus UAM Cantoblanco, 28049 Madrid, Spain.
Centro Nacional de Biotecnología · ES

Funding

NIMHD NIH HHS L60 MD002502
6 · The paper itself

Abstract

Primary cilia are involved in a variety of physiological processes such as sensing of the environment, cell growth and development. Numerous developmental disorders and pathologies arise from defects in these organelles. Multiple proteins that promote formation and disassembly of the primary cilium have been identified, but little is known about the mechanisms that control steady-state cilium size. Here, we show that death inducer obliterator (Dido3)-dependent targeting of histone deacetylase 6 (HDAC6) is a key determinant of cilium size in growth-arrested cells. The amount of either protein negatively correlates with cilium size. Dido3 availability at the centrosome governs ciliary HDAC6 levels, and redistribution of the two proteins controls tubulin acetylation. In turn, basal body localization of Dido3 and HDAC6 depends on the actin network, previously shown to limit cilium size independent of the cell cycle. These results show that not only kinase-dependent activation of a deacetylase but also its subcellular distribution controls substrate selection.

Indexed as

3T3 CellsAcetylationAnimalsBasal BodiesCell LineCentrosomeCiliaDNA-Binding ProteinsHistone Deacetylase 6Histone DeacetylasesMiceMicroscopy, ConfocalOrganelle SizeTranscription FactorsTubulinDido protein, mouseDNA-Binding ProteinsHdac6 protein, mouseHistone Deacetylase 6Histone DeacetylasesTranscription FactorsTubulin

Identifiers

PMID24667272
PMCPMC3973121
OpenAlexW2035823311

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.